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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2007-5-14
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pubmed:databankReference |
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pubmed:abstractText |
Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-10514371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-11522384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-11907243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-12384285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-12825167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-1328679,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-14610179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15163716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15165606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15596848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15795283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15805601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15890909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-15936661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-16254337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-16326711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-2177356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-6667333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-8035511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-8391187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-8749854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-9305654,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17392366-9914506
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5949-57
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17392366-ABO Blood-Group System,
pubmed-meshheading:17392366-Amino Acid Sequence,
pubmed-meshheading:17392366-Capsid Proteins,
pubmed-meshheading:17392366-Crystallization,
pubmed-meshheading:17392366-Crystallography, X-Ray,
pubmed-meshheading:17392366-Molecular Sequence Data,
pubmed-meshheading:17392366-Norovirus,
pubmed-meshheading:17392366-Oligosaccharides,
pubmed-meshheading:17392366-Protein Structure, Tertiary,
pubmed-meshheading:17392366-Receptors, Virus,
pubmed-meshheading:17392366-Trisaccharides
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pubmed:year |
2007
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pubmed:articleTitle |
Structural basis for the recognition of blood group trisaccharides by norovirus.
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pubmed:affiliation |
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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